VPS36_SCHPO
ID VPS36_SCHPO Reviewed; 467 AA.
AC O43038;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Vacuolar protein-sorting-associated protein 36;
GN Name=vps36; ORFNames=SPBC3B9.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=17660439; DOI=10.1099/mic.0.2007/006072-0;
RA Iwaki T., Onishi M., Ikeuchi M., Kita A., Sugiura R., Giga-Hama Y.,
RA Fukui Y., Takegawa K.;
RT "Essential roles of class E Vps proteins for sorting into multivesicular
RT bodies in Schizosaccharomyces pombe.";
RL Microbiology 153:2753-2764(2007).
CC -!- FUNCTION: Component of the ESCRT-II complex, which is required for
CC multivesicular body (MVB) formation and sorting of endosomal cargo
CC proteins into MVBs. The MVB pathway mediates delivery of transmembrane
CC proteins into the lumen of the lysosome for degradation. The ESCRT-II
CC complex is probably involved in the recruitment of the ESCRT-III
CC complex. Its ability to bind ubiquitin plays a central role in
CC endosomal sorting of ubiquitinated cargo proteins by the ESCRT
CC complexes (By similarity). Required for vacuolar sorting of
CC carboxypeptidase S (CPS). {ECO:0000250, ECO:0000269|PubMed:17660439}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex II (ESCRT-II). Binds ubiquitin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi
CC apparatus {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The second RanBP2-type zinc-finger is functional and binds
CC ubiquitin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17789.1; -; Genomic_DNA.
DR PIR; T40348; T40348.
DR RefSeq; NP_596667.1; NM_001022589.2.
DR AlphaFoldDB; O43038; -.
DR SMR; O43038; -.
DR BioGRID; 277497; 5.
DR STRING; 4896.SPBC3B9.09.1; -.
DR MaxQB; O43038; -.
DR PaxDb; O43038; -.
DR PRIDE; O43038; -.
DR EnsemblFungi; SPBC3B9.09.1; SPBC3B9.09.1:pep; SPBC3B9.09.
DR GeneID; 2540981; -.
DR KEGG; spo:SPBC3B9.09; -.
DR PomBase; SPBC3B9.09; vps36.
DR VEuPathDB; FungiDB:SPBC3B9.09; -.
DR eggNOG; KOG2760; Eukaryota.
DR HOGENOM; CLU_605754_0_0_1; -.
DR InParanoid; O43038; -.
DR OMA; YQNGHAY; -.
DR PhylomeDB; O43038; -.
DR Reactome; R-SPO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR PRO; PR:O43038; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000814; C:ESCRT II complex; ISO:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:PomBase.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:PomBase.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001876; Znf_RanBP2.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51495; GLUE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Golgi apparatus; Metal-binding; Protein transport;
KW Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Vacuolar protein-sorting-associated protein 36"
FT /id="PRO_0000373858"
FT DOMAIN 5..94
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 170..203
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT ZN_FING 97..122
FT /note="RanBP2-type 1; degenerate"
FT ZN_FING 137..161
FT /note="RanBP2-type 2"
SQ SEQUENCE 467 AA; 53178 MW; 1523145F2EEBCE41 CRC64;
MAFYLETTPS NLPVLDPSEE ILLVQDQVGL YFGDEKSFRH NNGTLYLTKK HIFYVDSVDP
KKNSLKIKIS DIRDVQHTSR YFRSSPKIRL SLRHVEKSWA CKICTFINVG DPINPCRNCG
VANRFTIIKP KSDARFSQGL CTACTFQNYP DLNTCEICGN QLKNVDRNQL IQLSFRGSGS
SKFYEAIKSE TDEIEKQRYS NKYDTKVLRK AILEKSLRMG GIHDLEQSHE MQLAKNGRTL
VHAFQDLDAF FSLAKDTMSL ADQFAEKMDG LTGTQQSDKV QQLLNKSNQL GVLRGNHLDN
VPVSANSRLY DIELCKSISE VLRTRLKADT DTVTMTQAWA IYNRSRKANL IPPTRFVKAC
ELIDSMEVGI TTSKMNSGLI LFQLKTSNHS GKLLSAILEV MNPSTTALKC AMRLHWSIGV
TLERLYQAEM DGYIVRDVYE ESGSSLLYWK NEFDELSEEL TKWFDES
